Amyloid-β and lysozyme proteotoxicity in Drosophila

Inks of different protein concentrations showed no significant variation of activity reduction and thus indicating the similar jetting ability of the linear range concentrations

Using a sensitive marker for neutrophil activation in peripheral blood, endogenous SAA in circulation lacked proinflammatory activity and thus differed functionally from

Amyloid and amyloid-like deposits are present in several known diseases including: Alzheimer’s disease, Parkinson’s disease, amyotrophic lateral sclerosis,

In the third part of this thesis, a fly model for lysozyme amyloidosis was used to study the effect of co-expressing the serum amyloid P component (SAP), a protein that is part of all

Our results demonstrate reduced propagation properties of Aβ aggregated in the presence of Aβ-seeds formed together with p-FTAA compared to Aβ-seeds formed without

1532, 2016 Department of Clinical and Experimental Medicine.

Using the Drosophila model of lysozyme amyloidosis that was established in paper I, the effects of expressing WT and the disease-associated lysozyme variant F57I in central

Abstract In this thesis Drosophila melanogaster the fruit fly has been used as a model organism to study the aggregation and toxic properties of the human amyloid β Aβ peptide